Structure of glutaminyl cyclase from Drosophila melanogaster in space group I4. Issue 4 (2nd April 2013)

• Record Type: Journal Article
• Authors: Kolenko, Petr; Koch, Birgit; Rahfeld, Jens‐Ulrich; Schilling, Stephan; Demuth, Hans‐Ulrich; Stubbs, Milton T.
• Is Part Of: Acta crystallographica. Volume 69:Issue 4(2013:Apr.)
• Page Start: 358
• Page End: 361
• Publication Date: 2013-04-02
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113005575
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The structure of ligand‐free glutaminyl cyclase (QC) from <italic>Drosophila melanogaster</italic> (<italic>Dm</italic>QC) has been determined in a novel crystal form. The protein crystallized in space group <italic>I</italic>4, with unit‐cell parameters <italic>a</italic> = <italic>b</italic> = 122.3, <italic>c</italic> = 72.7 Å. The crystal diffracted to a resolution of 2 Å at the home source. The structure was solved by molecular replacement and was refined to an <italic>R</italic> factor of 0.169. <italic>Dm</italic>QC exhibits a typical α/β‐hydrolase fold. The electron density of three monosaccharides could be localized. The accessibility of the active site will facilitate structural studies of novel inhibitor‐binding modes.</p> </abstract>